sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
1.940 Å
X-ray
2012-09-10
| Name: | Actin, alpha skeletal muscle |
|---|---|
| ID: | ACTS_RABIT |
| AC: | P68135 |
| Organism: | Oryctolagus cuniculus |
| Reign: | Eukaryota |
| TaxID: | 9986 |
| EC Number: | / |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| B | 100 % |
| B-Factor: | 31.979 |
|---|---|
| Number of residues: | 31 |
| Including | |
| Standard Amino Acids: | 28 |
| Non Standard Amino Acids: | 1 |
| Water Molecules: | 2 |
| Cofactors: | ATP |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 0.048 | 465.750 |
| % Hydrophobic | % Polar |
|---|---|
| 47.83 | 52.17 |
| According to VolSite | |
| HET Code: | LAR |
|---|---|
| Formula: | C22H31NO5S |
| Molecular weight: | 421.550 g/mol |
| DrugBank ID: | DB02621 |
| Buried Surface Area: | 64.94 % |
| Polar Surface area: | 110.16 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 6 |
| H-Bond Donors: | 2 |
| Rings: | 3 |
| Aromatic rings: | 0 |
| Anionic atoms: | 0 |
| Cationic atoms: | 0 |
| Rule of Five Violation: | 0 |
| Rotatable Bonds: | 1 |
| X | Y | Z |
|---|---|---|
| 10.1421 | -37.0604 | 25.0496 |
Image generated by PoseView
Represent the protein/ligand binding mode, centered on the ligand
Dashed lines represents hydrogen bonds and metal interactions
Green residue labels for amino acids with hydrophobic contacts (green lines) to the ligand
| Ligand | Protein | Interaction | |||
|---|---|---|---|---|---|
| Atom | Atom | Residue | Distance (Å) | Angle (°) | Type |
| C15 | CD2 | LEU- 16 | 3.8 | 0 | Hydrophobic |
| C14 | CB | PRO- 32 | 3.71 | 0 | Hydrophobic |
| C11 | CD1 | ILE- 34 | 4.46 | 0 | Hydrophobic |
| C12 | CG2 | ILE- 34 | 3.91 | 0 | Hydrophobic |
| C22 | CD1 | LEU- 67 | 3.52 | 0 | Hydrophobic |
| O3 | OH | TYR- 69 | 2.72 | 170.39 | H-Bond (Protein Donor) |
| C12 | CZ | TYR- 69 | 4.05 | 0 | Hydrophobic |
| C13 | CE2 | TYR- 69 | 4.35 | 0 | Hydrophobic |
| N1 | OD2 | ASP- 157 | 3.44 | 127.06 | H-Bond (Ligand Donor) |
| N1 | OD1 | ASP- 157 | 2.76 | 167.34 | H-Bond (Ligand Donor) |
| C19 | CG | ARG- 183 | 4.1 | 0 | Hydrophobic |
| S1 | CG2 | THR- 186 | 3.72 | 0 | Hydrophobic |
| O5 | OG1 | THR- 186 | 2.52 | 166.18 | H-Bond (Protein Donor) |
| S1 | CG | ARG- 206 | 3.44 | 0 | Hydrophobic |
| O4 | OE1 | GLU- 207 | 3.25 | 120.08 | H-Bond (Ligand Donor) |
| O4 | OE2 | GLU- 207 | 2.7 | 166.73 | H-Bond (Ligand Donor) |
| C22 | CG | GLU- 207 | 3.81 | 0 | Hydrophobic |
| S1 | CB | ARG- 210 | 4.02 | 0 | Hydrophobic |
| C17 | CD | ARG- 210 | 4.18 | 0 | Hydrophobic |
| O4 | NE | ARG- 210 | 3 | 123.34 | H-Bond (Protein Donor) |
